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| | ==Solution structure of the Sendai virus protein X C-subdomain== | | ==Solution structure of the Sendai virus protein X C-subdomain== |
| - | <StructureSection load='1r4g' size='340' side='right'caption='[[1r4g]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1r4g' size='340' side='right'caption='[[1r4g]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1r4g]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sendh Sendh]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R4G OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1R4G FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1r4g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sendai_virus_(strain_Harris) Sendai virus (strain Harris)]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R4G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R4G FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">P ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11196 SENDH])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1r4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r4g OCA], [https://pdbe.org/1r4g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r4g RCSB], [https://www.ebi.ac.uk/pdbsum/1r4g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r4g ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1r4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r4g OCA], [http://pdbe.org/1r4g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r4g RCSB], [http://www.ebi.ac.uk/pdbsum/1r4g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r4g ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PHOSP_SENDH PHOSP_SENDH]] Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template. Acts as a chaperone for newly synthesized free N protein, so-called N(0). Stabilizes the L protein upon binding it. | + | [https://www.uniprot.org/uniprot/PHOSP_SENDH PHOSP_SENDH] Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template. Acts as a chaperone for newly synthesized free N protein, so-called N(0). Stabilizes the L protein upon binding it. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: RNA-directed RNA polymerase]]
| + | [[Category: Blackledge M]] |
| - | [[Category: Sendh]]
| + | [[Category: Blanchard L]] |
| - | [[Category: Blackledge, M]] | + | [[Category: Burmeister WP]] |
| - | [[Category: Blanchard, L]] | + | [[Category: Marion D]] |
| - | [[Category: Burmeister, W P]] | + | [[Category: Ruigrok RW]] |
| - | [[Category: Marion, D]] | + | [[Category: Tarbouriech N]] |
| - | [[Category: Ruigrok, R W]] | + | [[Category: Timmins P]] |
| - | [[Category: Tarbouriech, N]] | + | |
| - | [[Category: Timmins, P]] | + | |
| - | [[Category: Three helix-bundle]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Viral protein]]
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| Structural highlights
Function
PHOSP_SENDH Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template. Acts as a chaperone for newly synthesized free N protein, so-called N(0). Stabilizes the L protein upon binding it.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The RNA-dependent RNA polymerase of the Sendai virus (SeV) consists of the large protein (L) and the phosphoprotein (P). P plays a crucial role in the enzyme by positioning L (which carries the polymerase activity) onto the matrix for transcription and replication formed by the RNA and the nucleoprotein, the N-RNA. P has a modular structure with distinct functional domains: an N-terminal domain involved in binding to N degrees (N that is not yet bound to RNA) and a C-terminal domain that carries the oligomerisation domain, the N-RNA binding domain and the L binding domain and that, combined with L, is active in transcription. Structural data have previously been obtained on the N-terminal domain and on the oligomerisation domain of P, but not yet on its N-RNA binding domain (also-called the X protein). Here we present an NMR and a small angle neutron scattering study of the SeV X protein. We show that this molecule presents two subdomains linked by an 11-residue linker, with the N-subdomain lacking a well-defined conformation. The 3D structure of the C-subdomain consists of three alpha-helices revealing an asymmetric charge distribution that may be important for binding to RNA-bound nucleoprotein. The structure of the entire C-terminal domain of P is modelled from its constituent parts in combination with small angle scattering data on this domain.
Structure and dynamics of the nucleocapsid-binding domain of the Sendai virus phosphoprotein in solution.,Blanchard L, Tarbouriech N, Blackledge M, Timmins P, Burmeister WP, Ruigrok RW, Marion D Virology. 2004 Feb 20;319(2):201-11. PMID:14980481[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Blanchard L, Tarbouriech N, Blackledge M, Timmins P, Burmeister WP, Ruigrok RW, Marion D. Structure and dynamics of the nucleocapsid-binding domain of the Sendai virus phosphoprotein in solution. Virology. 2004 Feb 20;319(2):201-11. PMID:14980481 doi:10.1016/j.virol.2003.10.029
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